› 4ivg

X-ray diffraction
1.75Å resolution

Crystal structure of mitochondrial Hsp90 (TRAP1) NTD-Middle domain dimer with AMPPNP

Released:
DOI: 10.2210/pdb4ivg/pdb
PDB entry 4ivg coloured by chain, front view.
PDB entry 4ivg coloured by chain, side view.
PDB entry 4ivg coloured by chain, top view.
Source organism: Danio rerio
Primary publication:
Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.
Lavery LA, Partridge JR, Ramelot TA, Elnatan D, Kennedy MA, Agard DA
Mol Cell 53 330-43 (2014)
PMID: 24462206

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-108806 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidine kinase/HSP90-like ATPase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 647 amino acids
Theoretical weight: 73.95 KDa
Source organism: Danio rerio
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A8WFV1 (Residues: 73-719; Coverage: 90%)
Gene names: fc85a11, trap1, wu:fc85a11
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand ANP 1 x ANP
Ligand PO4 1 x PO4
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: I222
Unit cell:
a: 85.146Å b: 94.509Å c: 155.456Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.203
Expression system: Escherichia coli BL21(DE3)

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Citations

31 review citations

The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology.
Bernardi et al. (2015)
30 more

5 mentions without citation

Structural asymmetry in the closed state of mitochondrial Hsp90 (TRAP1) supports a two-step ATP hydrolysis mechanism.
Lavery et al. (2014)
4 more